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Methods of Protein Iodination
Published in Erwin Regoeczi, Iodine-Labeled Plasma Proteins, 2019
Ishiguro and colleagues197 iodinated ricin at pH 7.0 using 90 mg of the protein and a 20- fold molar excess of iodine. The reagent contained 0.05 M I in 0.1 M KI, and it was added to the protein slowly over 15 min. Reactions took place for 1 hr in an ice bath. The main purpose of the study was to correlate the hemagglutinating activity (which was unchanged) and the toxicity of ricin (which was strongly reduced) with amino acid modifications. Substitutions were followed partly by the spectral changes of modified tyrosines and partly by the employment of 131I.
Chemistry
Published in Stephen P. Coburn, The Chemistry and Metabolism of 4′-Deoxypyridoxine, 2018
In a typical run, 600 mf of acetone was distilled directly into a 1000- mf round bottom flask containing 45 g pyridoxine hydrochloride. After cooling to 0°C in brine, dry hydrogen chloride was bubbled through a gas diffusion tube with stirring until a 15 to 17% solution was obtained. Stirring was continued for 30 min in the ice bath and for one hour at room temperature. The reaction can be monitored by chromatography and/or ultraviolet spectroscopy to verify that the phenol group is blocked. After standing overnight at 4°C, 400 ml of cold, dry ether was added to the cold suspension and the precipitate of isopropylidenepyridoxine hydrochloride was collected by filtration, washed with cold ether, and dried at 65°C for 2 hr (yield 50.4 g [94%]; M.P. 210 to 212°C [decomposition]).
Antidiabetic Activity by the In Vitro α-Amylase and α-Glucosidase Inhibitory Action of Indian Ayurvedic Medicinal Plants
Published in Parimelazhagan Thangaraj, Medicinal Plants, 2018
Karuppusamy Arunachalam, Puthanpura Sasidharan Sreeja, Domingos Tabajara de Oliveira Martins, Parimelazhagan Thangaraj
α-Amylase was premixed with extract at various concentrations (50–200 μg/mL) and starch as a substrate was added (0.5% starch solution) to start the reaction. The reaction was carried out at 37°C for 5 min and terminated by the addition of 2 mL of DNS (3,5-dinitrosalicylic acid) reagent. The reaction mixture was heated for 15 min at 100°C and diluted with 10 mL of distilled water in an ice bath (Miller 1959). α-Amylase activity was determined by measuring the spectrum at 540 nm. The IC50 value was defined as the concentration of α-amylase inhibitor to inhibit 50% of its activity under the assay conditions.
Mindfulness for the Moment: Adapting Interventions for the Period of the Sport Season
Published in Journal of Sport Psychology in Action, 2023
Andrew N. Augustus, Samuel Zizzi, Thomas Minkler, Christopher Lindauer
To begin, a consultant or coach could lead a discussion to help athletes re-connect to values and norms established by the team early in the season, and emphasize how athletes can apply previously learned mindfulness exercises into their days to optimize training and recovery. Starting practice with a consultant-led (or app-based) meditation and discussion emphasizing acceptance can help athletes gain more adaptive perspectives on pain (Jones & Parker, 2018) and to embrace challenges as opportunities to grow. Post-practice relaxation- or compassion-focused meditations could be led by consultants (or via apps) to help reinforce compassion for self and serve as passive recovery. Athletes could be encouraged to apply mindfulness concepts and exercises with other recovery methods prescribed by certified athletic trainers or strength coaches (e.g., focusing on breath and accepting discomfort during an ice bath). A mindful walk (via an app or self-guided) could help manage stress and promote well-being while they go to and from class or practice. By integrating these brief mindfulness exercises into practice, the training room, and daily routines, coaches and athletes are prioritizing physical and mental recovery during this period without adding additional time to a busy and stressful period.
Evaluation of the hepatoprotective effect of curcumin-loaded solid lipid nanoparticles against paracetamol overdose toxicity: Role of inducible nitric oxide synthase
Published in Journal of Liposome Research, 2022
Rasha M. Hussein, Mohamed A. Kandeil, Norhan A. Mohammed, Rasha A. Khallaf
SLNs were developed according to a previously reported method with modifications (Wang et al. 2010). In brief, the non-aqueous phase was prepared by dissolving fixed amounts of Cur (10 mg) and stearic acid (100 mg) and varying concentrations of lecithin (0.06, 0.125 and 0.25 5% w/v) into 10 ml of ethyl alcohol. Variable concentrations of P-188 (0.8. 1.6 and 2.4% w/v) were dissolved in 25 ml water forming the aqueous phase and both phases were heated to the same temperature (60 °C). Nanoparticles’ suspension was formulated by dropping the organic phase at a constant rate into the aqueous phase under homogenisation (8000 rpm, 15 min) using Heidolph high sheer homogeniser (Heidolph Diax 900, Germany) at the same temperature (60 °C) to ensure complete solvent removal. The Formed SLNs were instantly transferred to 25 ml of cold distilled water and stirred at 800 rpm for 1 h. in an ice bath. Free Cur was separated from entrapped one by centrifugation of the produced nano-suspension at 20000 rpm for 1 h. (Sigma cooling centrifuge, 3–30 K, Sigma-Elektro, Germany). The separated precipitate was washed twice, desiccated, and kept for further characterisation.
microRNA-17-5p downregulation inhibits autophagy and myocardial remodelling after myocardial infarction by targeting STAT3
Published in Autoimmunity, 2022
Bo Chen, Yingjun Yang, Jinbo Wu, Jianjiang Song, Jia Lu
Total RNA was extracted from myocardial tissues by Trizol one-step method according to the instructions of TRIzol (Invitrogen Inc., Carlsbad, CA) reagent. RNA was dissolved by ultrapure water treated with diethyl pyrocarbonate (DEPC). The absorbance at the wavelength of 260 nm and 280 nm was detected by an ultraviolet-visible spectrophotometer (ND-1000, NanoDrop Technologies, Wilmington, DE, USA). The quality of total RNA was checked and the concentration of total RNA was adjusted. The experimental conditions were as follows: at 70 °C for 10 min, ice-bath for 2 min, at 42 °C for 60 min, and at 70 °C for 10 min. The complementary DNA obtained from reverse transcription was preserved at −80 °C temporarily. RT-qPCR was operated by the TaqMan probe method in accordance with the instructions of the kits (Fermentas Inc., Vilnius, Lithuania). The RT-qPCR was performed on ABI 7500 instruments (ABI, Foster City, CA, USA) with U6 as an internal control. The relative expression was determined with the 2−ΔΔCT method. Primer sequences are illustrated in Table 1.